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PDBsum entry 3ghg
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Blood clotting
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PDB id
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3ghg
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Contents |
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174 a.a.
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401 a.a.
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381 a.a.
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186 a.a.
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References listed in PDB file
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Key reference
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Title
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Crystal structure of human fibrinogen.
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Authors
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J.M.Kollman,
L.Pandi,
M.R.Sawaya,
M.Riley,
R.F.Doolittle.
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Ref.
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Biochemistry, 2009,
48,
3877-3886.
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PubMed id
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Abstract
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A crystal structure of human fibrinogen has been determined at approximately 3.3
A resolution. The protein was purified from human blood plasma, first by a cold
ethanol precipitation procedure and then by stepwise chromatography on
DEAE-cellulose. A product was obtained that was homogeneous on
SDS-polyacrylamide gels. Nonetheless, when individual crystals used for X-ray
diffraction were examined by SDS gel electrophoresis after data collection, two
species of alpha chain were present, indicating that some proteolysis had
occurred during the course of operations. Amino-terminal sequencing on
post-X-ray crystals showed mostly intact native alpha- and gamma-chain sequences
(the native beta chain is blocked). The overall structure differs from that of a
native fibrinogen from chicken blood and those reported for a partially
proteolyzed bovine fibrinogen in the nature of twist in the coiled-coil regions,
likely due to weak forces imparted by unique crystal packing. As such, the
structure adds to the inventory of possible conformations that may occur in
solution. Other features include a novel interface with an antiparallel
arrangement of beta chains and a unique tangential association of coiled coils
from neighboring molecules. The carbohydrate groups attached to beta chains are
unusually prominent, the full sweep of 11 sugar residues being positioned. As
was the case for native chicken fibrinogen, no resolvable electron density could
be associated with alphaC domains.
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